Reviewed, UniProtKB/Swiss-Prot O00418 (EF2K_HUMAN)

Names and origin

Protein names

Recommended name:
    Elongation factor 2 kinase
    EC=2.7.11.20
Alternative name(s):
    eEF-2 kinase
      Short name=eEF-2K
    Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase

Gene names

Name:

EEF2K

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates eukaryotic elongation factor-2. Binds calmodulin By similarity.
Catalytic activity	ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate.
Enzyme regulation	Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent By similarity.
Subunit structure	Monomer or homodimer Potential.
Sequence similarities	Belongs to the protein kinase superfamily. Alpha-type protein kinase family. Contains 1 alpha-type protein kinase domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro translational elongation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW elongation factor-2 kinase activity Inferred from electronic annotation. Source: EC translation factor activity, nucleic acid binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 725	725	Elongation factor 2 kinase		PRO_0000086936
Regions
	Domain	116 – 326	211	Alpha-type protein kinase
	Nucleotide binding	296 – 302	7	ATP By similarity
	Region	594 – 610	17	Calmodulin-binding Potential
	Region	610 – 627	18	Pseudosubstrate/autoinhibitory domain Potential
Amino acid modifications
	Modified residue	18	1	Phosphoserine Ref.3 Ref.4 Ref.5 Ref.7
	Modified residue	27	1	Phosphoserine Ref.4
	Modified residue	31	1	Phosphoserine Ref.4
	Modified residue	69	1	Phosphotyrosine Ref.4
	Modified residue	70	1	Phosphoserine Ref.4
	Modified residue	71	1	Phosphoserine By similarity
	Modified residue	135	1	Phosphoserine Ref.6
	Modified residue	348	1	Phosphothreonine Ref.7
	Modified residue	445	1	Phosphoserine Ref.5
	Modified residue	470	1	Phosphoserine Ref.4 Ref.7
	Modified residue	474	1	Phosphoserine Ref.4 Ref.7
	Modified residue	477	1	Phosphoserine Ref.7
Natural variations
	Natural variant	23	1	H → R: dbSNP rs9935059. Ref.2 Ref.9		VAR_033915
	Natural variant	75	1	P → A: dbSNP rs17841292. Ref.9		VAR_033916
	Natural variant	291	1	T → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.9		VAR_041534
	Natural variant	433	1	R → W Ref.9		VAR_041535
	Natural variant	609	1	D → H Ref.9		VAR_041536

Sequences

	Sequence		Length	Mass (Da)
	O00418-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: E006FECAF169F70D	FASTA	725	82,172
	10 20 30 40 50 60 MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ NVNSKVNKYY 70 80 90 100 110 120 SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA EFHLEDIATE RATRHRYNAV 130 140 150 160 170 180 TGEWLDDEVL IKMASQPFGR GAMRECFRTK KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV 190 200 210 220 230 240 YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN 250 260 270 280 290 300 SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL 310 320 330 340 350 360 GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL RGTEEKCGSP 370 380 390 400 410 420 RVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA TPHSQKLDHL HWPVFSDLDN 430 440 450 460 470 480 MASRDHDHLD NHRESENSGD SGYPSEKRGE LDDPEPREHG HSYSNRKYES DEDSLGSSGR 490 500 510 520 530 540 VCVEKWNLLN SSRLHLPRAS AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC 550 560 570 580 590 600 EKGEEWDQES AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY 610 620 630 640 650 660 LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC DEGGEYDGMQ 670 680 690 700 710 720 DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA MEAMKGRLAN QYYQKAEEAW AQMEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase." Ryazanov A.G., Ward M.D., Mendola C.E., Pavur K.S., Dorovkov M.V., Wiedmann M., Erdjument-Bromage H., Tempst P., Parmer T.G., Prostko C.R., Germino F.J., Hait W.N. Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997) [PubMed: 9144159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Glial tumor.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-23. Tissue: Lymph.
[3]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: T-cell.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-27; SER-31; TYR-69; SER-70; SER-470 AND SER-474, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, MASS SPECTROMETRY.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-348; SER-470; SER-474 AND SER-477, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-23; ALA-75; MET-291; TRP-433 AND HIS-609.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U93850 mRNA. Translation: AAB58270.1. BC032665 mRNA. Translation: AAH32665.1.
IPI	IPI00011689.
RefSeq	NP_037434.1.
UniGene	Hs.633744
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	O00418.
Proteomic databases
PRIDE	O00418.
Genome annotation databases
Ensembl	ENSG00000103319. Homo sapiens. [Contig view]
GeneID	29904.
KEGG	hsa:29904.
Organism-specific databases
GeneCards	GC16P022125.
H-InvDB	HIX0021510.
HGNC	HGNC:24615. EEF2K.
HPA	CAB007818.
MIM	606968. gene.
PharmGKB	PA134992891.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O00418.
HOVERGEN	O00418.
Enzyme and pathway databases
BRENDA	2.7.11.20. 247.
Pathway_Interaction_DB	p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.
Reactome	REACT_498. Signaling by Insulin receptor.
Gene expression databases
ArrayExpress	O00418.
Bgee	O00418.
CleanEx	HS_EEF2K.
GermOnline	ENSG00000103319. Homo sapiens.
Family and domain databases
InterPro	IPR017400. Elongation_factor_2_kinase. IPR004166. MHCK_EF2_kinase. IPR006597. Sel1-like. IPR011990. TPR-like_helical. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
Pfam	PF02816. Alpha_kinase. 1 hit. PF08238. Sel1. 3 hits. [Graphical view]
PIRSF	PIRSF038139. Elongation_factor_2_kinase. 1 hit.
SMART	SM00811. Alpha_kinase. 1 hit. [Graphical view]
PROSITE	PS51158. ALPHA_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	52478.
SOURCE	Search...

Entry information

Entry name

EF2K_HUMAN

Accession

Primary (citable) accession number: O00418
Secondary accession number(s): Q8N588

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)